IHOG_DROME
ID IHOG_DROME Reviewed; 886 AA.
AC Q9VM64; C0PTX1; Q2XY56;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Interference hedgehog {ECO:0000303|PubMed:16630821};
DE Flags: Precursor;
GN Name=ihog; ORFNames=CG9211;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000312|EMBL:AAF52461.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF52461.1}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAM50119.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM50119.1};
RC TISSUE=Head {ECO:0000269|PubMed:16120803};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305, ECO:0000312|EMBL:ABA86412.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-880.
RC STRAIN=Ral1 {ECO:0000312|EMBL:ABA86412.1};
RX PubMed=16120803; DOI=10.1093/molbev/msi246;
RA Comeron J.M., Guthrie T.B.;
RT "Intragenic Hill-Robertson interference influences selection intensity on
RT synonymous mutations in Drosophila.";
RL Mol. Biol. Evol. 22:2519-2530(2005).
RN [5] {ECO:0000305, ECO:0000312|EMBL:ACN58579.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 21-711.
RC STRAIN=Berkeley;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP IDENTIFICATION.
RX PubMed=12663920; DOI=10.1126/science.1081403;
RA Lum L., Yao S., Mozer B., Rovescalli A., Von Kessler D., Nirenberg M.,
RA Beachy P.A.;
RT "Identification of Hedgehog pathway components by RNAi in Drosophila
RT cultured cells.";
RL Science 299:2039-2045(2003).
RN [7] {ECO:0000305}
RP FUNCTION, INTERACTION WITH HH, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP DOMAIN, AND DISRUPTION PHENOTYPE.
RX PubMed=16630821; DOI=10.1016/j.cell.2006.02.040;
RA Yao S., Lum L., Beachy P.A.;
RT "The ihog cell-surface proteins bind Hedgehog and mediate pathway
RT activation.";
RL Cell 125:343-357(2006).
RN [8] {ECO:0000305}
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-108, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [9] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 466-677 IN A COMPLEX WITH HH,
RP SUBUNIT, HEPARIN-BINDING, AND MUTAGENESIS OF ARG-503; LYS-507; LYS-509 AND
RP ARG-547.
RX PubMed=17077139; DOI=10.1073/pnas.0606738103;
RA McLellan J.S., Yao S., Zheng X.H., Geisbrecht B.V., Ghirlando R.,
RA Beachy P.A., Leahy D.J.;
RT "Structure of a heparin-dependent complex of Hedgehog and Ihog.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:17208-17213(2006).
CC -!- FUNCTION: Mediates response to the active Hedgehog (Hh) protein signal
CC in embryos, functioning upstream or at the level of patched (ptc).
CC {ECO:0000269|PubMed:16630821}.
CC -!- SUBUNIT: Homodimer. Heterotetramer; 2 iHog chains bind 2 hh chains when
CC facilitated by heparin, heparin is required to promote high-affinity
CC interactions between hh and iHog. {ECO:0000269|PubMed:16630821,
CC ECO:0000269|PubMed:17077139}.
CC -!- INTERACTION:
CC Q9VM64; Q02936-1: hh; NbExp=6; IntAct=EBI-94134, EBI-15609026;
CC Q9VM64; Q9VM64: ihog; NbExp=3; IntAct=EBI-94134, EBI-94134;
CC Q9VM64; Q94918: vn; NbExp=2; IntAct=EBI-94134, EBI-869384;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255, ECO:0000269|PubMed:16630821}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:16630821}.
CC -!- DOMAIN: The first Fibronectin type-III domain mediates a specific
CC interaction with Hh protein, in vitro. The second Fibronectin type-III
CC domain is additionally required for in vivo signaling activity.
CC {ECO:0000269|PubMed:16630821}.
CC -!- DISRUPTION PHENOTYPE: Patterning defects characteristic of Hh signaling
CC loss in embryos and imaginal disks. {ECO:0000269|PubMed:16630821}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. IHOG family.
CC {ECO:0000255}.
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DR EMBL; AE014134; AAF52461.1; -; Genomic_DNA.
DR EMBL; AY119465; AAM50119.1; -; mRNA.
DR EMBL; DQ138806; ABA86412.1; -; Genomic_DNA.
DR EMBL; BT071816; ACN58579.1; -; mRNA.
DR RefSeq; NP_609085.1; NM_135241.2.
DR PDB; 2IBB; X-ray; 2.40 A; A=466-676.
DR PDB; 2IBG; X-ray; 2.20 A; A/B/C/D=466-677.
DR PDB; 2IC2; X-ray; 1.30 A; A/B=466-577.
DR PDBsum; 2IBB; -.
DR PDBsum; 2IBG; -.
DR PDBsum; 2IC2; -.
DR AlphaFoldDB; Q9VM64; -.
DR SMR; Q9VM64; -.
DR BioGRID; 60122; 8.
DR DIP; DIP-35774N; -.
DR IntAct; Q9VM64; 4.
DR STRING; 7227.FBpp0078993; -.
DR GlyGen; Q9VM64; 5 sites.
DR iPTMnet; Q9VM64; -.
DR PaxDb; Q9VM64; -.
DR PRIDE; Q9VM64; -.
DR DNASU; 33972; -.
DR EnsemblMetazoa; FBtr0079365; FBpp0078993; FBgn0031872.
DR GeneID; 33972; -.
DR KEGG; dme:Dmel_CG9211; -.
DR UCSC; CG9211-RA; d. melanogaster.
DR CTD; 33972; -.
DR FlyBase; FBgn0031872; ihog.
DR VEuPathDB; VectorBase:FBgn0031872; -.
DR eggNOG; ENOG502QSGM; Eukaryota.
DR GeneTree; ENSGT00940000172763; -.
DR HOGENOM; CLU_004633_1_0_1; -.
DR InParanoid; Q9VM64; -.
DR OMA; CGLMEGK; -.
DR OrthoDB; 102649at2759; -.
DR PhylomeDB; Q9VM64; -.
DR Reactome; R-DME-209338; Assembly of the 'signalling complexes'.
DR Reactome; R-DME-373752; Netrin-1 signaling.
DR Reactome; R-DME-376176; Signaling by ROBO receptors.
DR Reactome; R-DME-418885; DCC mediated attractive signaling.
DR Reactome; R-DME-418889; Caspase activation via Dependence Receptors in the absence of ligand.
DR Reactome; R-DME-428542; Regulation of commissural axon pathfinding by SLIT and ROBO.
DR SignaLink; Q9VM64; -.
DR BioGRID-ORCS; 33972; 0 hits in 3 CRISPR screens.
DR EvolutionaryTrace; Q9VM64; -.
DR GenomeRNAi; 33972; -.
DR PRO; PR:Q9VM64; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0031872; Expressed in eye disc (Drosophila) and 26 other tissues.
DR ExpressionAtlas; Q9VM64; baseline and differential.
DR Genevisible; Q9VM64; DM.
DR GO; GO:0044295; C:axonal growth cone; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; IDA:FlyBase.
DR GO; GO:0035230; C:cytoneme; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015026; F:coreceptor activity; IGI:FlyBase.
DR GO; GO:0097108; F:hedgehog family protein binding; IDA:FlyBase.
DR GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005113; F:patched binding; IPI:FlyBase.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0048749; P:compound eye development; IGI:FlyBase.
DR GO; GO:0035017; P:cuticle pattern formation; IMP:FlyBase.
DR GO; GO:0034109; P:homotypic cell-cell adhesion; IDA:FlyBase.
DR GO; GO:0071694; P:maintenance of protein location in extracellular region; IGI:FlyBase.
DR GO; GO:0001764; P:neuron migration; IBA:GO_Central.
DR GO; GO:0007379; P:segment specification; IMP:FlyBase.
DR GO; GO:0007224; P:smoothened signaling pathway; IDA:FlyBase.
DR GO; GO:0048100; P:wing disc anterior/posterior pattern formation; IGI:FlyBase.
DR GO; GO:0035222; P:wing disc pattern formation; IMP:FlyBase.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF13895; Ig_2; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 3.
DR SUPFAM; SSF48726; SSF48726; 3.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Heparin-binding;
KW Immunoglobulin domain; Membrane; Proteoglycan; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..886
FT /note="Interference hedgehog"
FT /evidence="ECO:0000255"
FT /id="PRO_0000383615"
FT TOPO_DOM 21..709
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 710..730
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 731..886
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 51..148
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255"
FT DOMAIN 138..238
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255"
FT DOMAIN 258..346
FT /note="Ig-like C2-type 3"
FT /evidence="ECO:0000255"
FT DOMAIN 352..438
FT /note="Ig-like C2-type 4"
FT /evidence="ECO:0000255"
FT DOMAIN 467..573
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 581..676
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 29..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 503
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000269|PubMed:17077139"
FT BINDING 507
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000269|PubMed:17077139"
FT BINDING 509
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000269|PubMed:17077139"
FT BINDING 547
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000269|PubMed:17077139"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 563
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 699
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 74..132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 179..226
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 282..330
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 373..420
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MUTAGEN 503
FT /note="R->E: Loss of Heparin binding."
FT /evidence="ECO:0000269|PubMed:17077139"
FT MUTAGEN 507
FT /note="K->E: Loss of Heparin binding."
FT /evidence="ECO:0000269|PubMed:17077139"
FT MUTAGEN 509
FT /note="K->E: Loss of Heparin binding."
FT /evidence="ECO:0000269|PubMed:17077139"
FT MUTAGEN 547
FT /note="R->E: Loss of Heparin binding."
FT /evidence="ECO:0000269|PubMed:17077139"
FT CONFLICT 47..49
FT /note="Missing (in Ref. 4; ABA86412)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="S -> L (in Ref. 4; ABA86412)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="E -> D (in Ref. 4; ABA86412)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="E -> Q (in Ref. 4; ABA86412)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="N -> H (in Ref. 4; ABA86412)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="K -> E (in Ref. 4; ABA86412)"
FT /evidence="ECO:0000305"
FT STRAND 472..475
FT /evidence="ECO:0007829|PDB:2IC2"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:2IBB"
FT STRAND 481..488
FT /evidence="ECO:0007829|PDB:2IC2"
FT STRAND 495..504
FT /evidence="ECO:0007829|PDB:2IC2"
FT STRAND 512..519
FT /evidence="ECO:0007829|PDB:2IC2"
FT STRAND 522..524
FT /evidence="ECO:0007829|PDB:2IBG"
FT STRAND 526..537
FT /evidence="ECO:0007829|PDB:2IC2"
FT STRAND 542..554
FT /evidence="ECO:0007829|PDB:2IC2"
FT STRAND 559..561
FT /evidence="ECO:0007829|PDB:2IC2"
FT STRAND 568..570
FT /evidence="ECO:0007829|PDB:2IC2"
FT STRAND 573..575
FT /evidence="ECO:0007829|PDB:2IBB"
FT STRAND 591..593
FT /evidence="ECO:0007829|PDB:2IBG"
FT STRAND 595..600
FT /evidence="ECO:0007829|PDB:2IBG"
FT HELIX 607..609
FT /evidence="ECO:0007829|PDB:2IBG"
FT STRAND 612..619
FT /evidence="ECO:0007829|PDB:2IBG"
FT STRAND 627..632
FT /evidence="ECO:0007829|PDB:2IBG"
FT STRAND 638..641
FT /evidence="ECO:0007829|PDB:2IBG"
FT STRAND 649..657
FT /evidence="ECO:0007829|PDB:2IBG"
FT STRAND 669..672
FT /evidence="ECO:0007829|PDB:2IBG"
SQ SEQUENCE 886 AA; 97846 MW; 8DA038FA9107E227 CRC64;
MTLLTSSLLL FSLLTSRLEA IPVLEKSPAH PAHSAHPAHP AHPAHPAHPS PGVRILRAPE
SLVAPLGDEV VLECETSLQP ERFEWSHRSS RSPGAGFKYL KTGTAKANVS QEAAISRLRV
LVRPDTLGEY RCVGWFGPLV VTSTIARLEL ASTSLVDAQE SESPLQWRVS AGNSVLWSCG
QQVQSNPSAS WSYYRNGVEI KPEFIGTNGN LFLSNVSSES SGSYSCQATN PASGERIQLP
GSLQLQVTPE QRSESKSPHL LRGQPSSQEI TIREGSSLLL LCPGVGSPPP TVVWSSPDVV
GAVKNKRSKV FGHALEISNT RVNDAGTYIC FQDNGVRPAL EHYIKVHVEQ PPQIVRPPWA
DLTNEGDRLK LECKATGVPT PEIYWLLNGH SSIDDSEAEL SNNFLILHSV LKRHAGYVQC
FARNRLGEHS AGTLLQVNPK QIQEPRESGG THRPKPNQGS RQKQMYPPTP PNVTRLSDES
VMLRWMVPRN DGLPIVIFKV QYRMVGKRKN WQTTNDNIPY GKPKWNSELG KSFTASVTDL
KPQHTYRFRI LAVYSNNDNK ESNTSAKFYL QPGAALDPMP VPELLEIEEY SETAVVLHWS
LASDADEHLI TGYYAYYRPS SSAGEYFKAT IEGAHARSFK IAPLETATMY EFKLQSFSAA
SASEFSALKQ GRTQRPKTST TEEPTLQMGD RDTTTPSHNE TFNMSPMLTG TIGGGAVLIL
LLISTCFCVC RRRNSRSRGN NPNKPRMAEL RDDFVPLGNC SPTKQRQRTR HIHITLNPLA
QQQQQALEEK NDTDQDAPYY QRPSSYDYDP TLRRMSSSSL RRSQRTLERA GGSNGSNNGN
NNNLNQSAEA GSIENPGKPG RVLMKRPRLS SRSENLSSGS LNSVGV
